ArticleACS chemical biology2015
Nonenzymatic Protein Acetylation Detected by NAPPA Protein Arrays.
Article in ACS chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
27 citing papers in PubMed, 43 citations in OpenAlex.
- The roles of the acetyltransferase domains of the chromatin regulators KAT6A and KAT6B in vivo.Development (Cambridge, England) · 2026Article
- Mitochondrial hyper-acetylation induced by an engineered acetyltransferase promotes cellular senescence.iScience · 2025Article
- Influence of the Microbial Metabolite Acetyl Phosphate on Mitochondrial Functions Under Conditions of Exogenous Acetylation and Alkalization.Metabolites · 2024Article
- Epigenetic meets metabolism: novel vulnerabilities to fight cancer.Cell communication and signaling : CCS · 2023Review
- Acetyl-CoA-mediated autoacetylation of fatty acid synthase as a metabolic switch of de novo lipogenesis inProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Non-enzymatic Covalent Modifications as a New Chapter in the Histone Code.Trends in biochemical sciences · 2021Review
- Ready, SET, Go: Post-translational regulation of the histone lysine methylation network in budding yeast.The Journal of biological chemistry · 2021Review
- Catalysis by protein acetyltransferase Gcn5.Biochimica et biophysica acta. Gene regulatory mechanisms · 2021Review
- Post-translational Lysine Ac(et)ylation in Bacteria: A Biochemical, Structural, and Synthetic Biological Perspective.Frontiers in microbiology · 2021Review
- Compartmentalised acyl-CoA metabolism and roles in chromatin regulation.Molecular metabolism · 2020Review
- Revealing Dynamic Protein Acetylation across Subcellular Compartments.Journal of proteome research · 2020Article
- Enzymatic and nonenzymatic protein acetylations control glycolysis process in liver diseases.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Review
- (De)Toxifying the Epigenetic Code.Chemical research in toxicology · 2019Review
- Biochemical and structural analysis of N-terminal acetyltransferases.Methods in enzymology · 2019Article
- Characterization of histone acylations links chromatin modifications with metabolism.Nature communications · 2017Article
- Proteome-wide acetylation dynamics in human cells.Scientific reports · 2017Article
- Discovering Targets of Non-enzymatic Acylation by Thioester Reactivity Profiling.Cell chemical biology · 2017Article
- Comprehensive Proteomic Analysis of Lysine Acetylation in the Foodborne PathogenFrontiers in microbiology · 2017Article
- Metabolic control of epigenetics in cancer.Nature reviews. Cancer · 2016Review
- A Microwell-Printing Fabrication Strategy for the On-Chip Templated Biosynthesis of Protein Microarrays for Surface Plasmon Resonance Imaging.The journal of physical chemistry. C, Nanomaterials and interfaces · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
Acetylation is a post-translational modification that occurs on thousands of proteins located in many cellular organelles. This process mediates many protein functions and modulates diverse biological processes. In mammalian cells, where acetyl-CoA is the primary acetyl donor, acetylation in the mitochondria is thought to occur by chemical means due to the relatively high concentration of acetyl-CoA located in this organelle. In contrast, acetylation outside of the mitochondria is thought to be mediated predominantly by acetyltransferase enzymes. Here, we address the possibility that nonenzymatic chemical acetylation outside of the mitochondria may be more common than previously appreciated. We employed the Nucleic Acid Programmable Protein Array platform to perform an unbiased screen for human proteins that undergo chemical acetylation, which resulted in the identification of a multitude of proteins with diverse functions and cellular localization. Mass spectrometry analysis revealed that basic residues typically precede the acetylated lysine in the -7 to -3 position, and we show by mutagenesis that these basic residues contribute to chemical acetylation capacity. We propose that these basic residues lower the pKa of the substrate lysine for efficient chemical acetylation. Many of the identified proteins reside outside of the mitochondria and have been previously demonstrated to be acetylated in vivo. As such, our studies demonstrate that chemical acetylation occurs more broadly throughout the eukaryotic cell than previously appreciated and suggests that this post-translational protein modification may have more diverse roles in protein function and pathway regulation.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.